Topic
Polyglutamylation
About: Polyglutamylation is a research topic. Over the lifetime, 213 publications have been published within this topic receiving 10877 citations. The topic is also known as: Polyglutamylation.
Papers published on a yearly basis
Papers
TL;DR: Functional studies demonstrating that post-translational modifications may regulate microtubule functions through an amazing range of mechanisms are demonstrated.
Abstract: Cells generate distinct microtubule subtypes by expressing different tubulin isotypes and through tubulin post-translational modifications, such as detyrosination, acetylation, polyglutamylation and polyglycylation The recent discovery of enzymes responsible for many of these modifications has shown how they may regulate microtubule functions
823 citations
TL;DR: A posttranslational modification consisting of the successive addition of glutamyl units on the gamma-carboxyl group of a glutamate residue (Glu445) could play a role in regulating microtubule dynamics.
Abstract: The high degree of tubulin heterogeneity in neurons is controlled mainly at the posttranslational level. Several variants of alpha-tubulin can be posttranslationally labeled after incubation of cells with [3H]acetate or [3H]glutamate. Peptides carrying the radioactive moiety were purified by high-performance liquid chromatography. Amino acid analysis, Edman degradation sequencing, and mass spectrometric analysis of these peptides led to the characterization of a posttranslational modification consisting of the successive addition of glutamyl units on the gamma-carboxyl group of a glutamate residue (Glu445). This modification, localized within a region of alpha-tubulin that is important in the interactions of tubulin with microtubule-associated proteins and calcium, could play a role in regulating microtubule dynamics.
545 citations
TL;DR: The results reveal that controlling the length of the polyglutamate side chains on tubulin is critical for neuronal survival and is directly linked to neurodegeneration.
353 citations
TL;DR: The neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase–like protein, TTLL1, a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates.
Abstract: Polyglutamylation of tubulin has been implicated in several functions of microtubules, but the identification of the responsible enzyme(s) has been challenging. We found that the neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase–like (TTLL) protein, TTLL1. TTLL1 is a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates. In the model protist Tetrahymena thermophila , two conserved types of polyglutamylases were characterized that differ in substrate preference and subcellular localization.
343 citations
Journal Article•
TL;DR: Results indicate that, in addition to alpha and beta' (class III)-tubulin, other beta-tubulin isotypes are also glutamylated, and this antibody has been used to analyze the cell and tissue distributions of glutamelated tubulin.
296 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 8 |
| 2020 | 10 |
| 2019 | 13 |
| 2018 | 9 |
| 2017 | 4 |
| 2016 | 8 |